RuBisCO

spinqualitylabelsall models PDB ID 1rcx Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
Spinach RuBisCO 8 large and 8 small chains complex with substrate ribulose-1,5- bisphosphate, 1rcx
Ligands:
Activity:	Ribulose-bisphosphate carboxylase, with EC number 4.1.1.39
Structural annotation: Resources: CATH : 1Rcxb02, 1Rcxb01, 1Rcxc00, 1Rcxe01, 1Rcxe02, 1Rcxf00, 1Rcxh02, 1Rcxh01, 1Rcxi00, 1Rcxk02, 1Rcxk01, 1Rcxl01, 1Rcxl02, 1Rcxm00, 1Rcxo02, 1Rcxo01, 1Rcxp00, 1Rcxr02, 1Rcxr01, 1Rcxs00, 1Rcxt00, 1Rcxv01, 1Rcxv02, 1Rcxw00 InterPro : Ipr000685, Ipr000894 Pfam : PF00016, PF02788, PF00101 SCOP : d1rcxb2, d1rcxb1, d1rcxc_, d1rcxe2, d1rcxe1, d1rcxf_, d1rcxh2, d1rcxh1, d1rcxi_, d1rcxk2, d1rcxk1, d1rcxl2, d1rcxl1, d1rcxm_, d1rcxo2, d1rcxo1, d1rcxp_, d1rcxr1, d1rcxr2, d1rcxs_, d1rcxt_, d1rcxv2, d1rcxv1, d1rcxw_ UniProt : P00875, P00870
Functional annotation: Cellular component: chloroplast chloroplast ribulose bisphosphate carboxylase complex Biological process: carbon utilization by fixation of carbon dioxide photosynthesis photorespiration reductive pentose-phosphate cycle Molecular function: lyase activity magnesium ion binding metal ion binding ribulose-bisphosphate carboxylase activity monooxygenase activity oxidoreductase activity
Evolutionary conservation: Toggle Conservation Colors: Rows = identical sequences: Further Information: Caveats, Explanation, Complete Results at ConSurfDB
Resources:	FirstGlance, OCA, PDBsum, RCSB
Coordinates:	save as pdb, mmCIF, xml

Ribulose-1,5-bisphosphate carboxylase oxygenase – RuBisCO (RBCO) catalyzes the first step in photosynthetic carbon fixation, and it is the most abundant protein on earth. RBCO can either carboxylate or oxygenate ribulose-1,5-bisphosphate (RUBP) with CO₂ or O₂, respectively. RBCO from flowering plants consists of eight large subunits and eight small subunits. Some additional details can be found in Ribulose-1,5-bisphosphate carboxylase/oxygenase.

Quaternery StructureQuaternery Structure

The Rubisco is shown in spacefill with its 8 large subunits in shades of blue and and its 8 small subunits in shades of yellow. The large subunits are arranged in head-to-toe pairs like staves in a barrel and the small subunits are arranged at the ends of the barrel. The large subunits contain the active sites and the function of the small subunits is not understood.

Large Subunit StructureLarge Subunit Structure

Here is an isolated . Each subunit has a large C-terminal lobe and a small N-terminal lobe, and the subunits are arranged head-to-toe (antiparallel) in the pair. are located in the interface of the large subunit pair. The subunits are shown in cartoon with one shown in the secondary structure color scheme. Each active site is occupied by RUBP, which is shown in CPK spacefill. Here is a showing that both lobes contain alpha helices (pink) and beta strands (yellow). The large lobe is dominated by an (amino acids 166-409), which contributes most of the residues that form the the active site. One residue from the N-terminal lobe of the adjacent large subunit completes the active site. This scene shows RUBP in spacefill and CPK in one of the active sites in the dimer. Both subunits are shown in transparent cartoon with the α-β barrel is pink and yellow. Asn 123 from the adjacent subunit is in blue spacefill, and residues 121-129 are shown in blue cartoon. This residue does not contribute to catalysis, and it will not be considered further.

Active Site StructureActive Site Structure

(under construction)

This scene shows an (cartoon and colored for secondary structure) of spinach Rubisco 8ruc, bound to the naturally occurring inhibitor 2-carboxylarabinitol-1,5-bisphosphate (2-CABP) and Mg²⁺, both shown in CPK spacefill. 2-CABP sits at one end of the α-β barrel, only residues from the beta strands and loops that link them to helices contribute to the active site.

3D Structures of RuBisCO3D Structures of RuBisCO

Updated February 2013

RuBisCORuBisCO

3rg6, 1rbl – SeRBCO – Synechococcus elongatus
2ybv - RBCO – Thermosynechococcus elongatus
3qfw - RBCO large subunit – Rhodopseudomonas palustris
1uzh, 1gk8 – CrRBCO – Chlamydomonas reinhardtii
1uw9, 1uwa – CrRBCO (mutant)
1svd – RBCD – Halothiobacillus neapolitanus
1bxn – RBCO – Cupriavidus necator
1aus - spRBCO – spinach
1rba - RrRBCO (mutant) – Rhododpirillum rubrum
5rub - RrRBCO
2wvw – RBCO – Anabena – Cryo EM
2vdh, 2vdi, 2v67, 2v68, 2v63, 2v69, 2v6a - CrRBCO (mutant)
1mlv - pRBCO LSMT – pea
2cxe, 2cwx – PhRBCO - Pyrococcus horikoshii
1uzd – CrRBCO/spRBCO
1geh – TkRBCO – Thermococcus kodakaraensis
1iwa - GpRBCO – Galdieria partita
1tel – RBCO large subunit – Chlorobium tepidum
1rld, 3rub, 3t15, 3zw6, 4rub – tRBCO – tobacco
3thg – RBCO – creosote bush
4hhh – RBCO - pea

RuBisCO complex with inhibitor 2-CABPRuBisCO complex with inhibitor 2-CABP

3kdn, 3a12 – TkRBCO III + 2-CABP
3kdo, 3a13 - TkRBCO III (mutant) + 2-CABP
1ir2 - CrRBCO + 2-CABP
1upm, 1upp, 1rbo, 3ruc, 8ruc - spRBCO + 2-CABP + cation
1ir1 - spRBCO + 2-CABP + CO2 + Mg
1wdd – rRBCO + 2-CABP – rice
1bwv - GpRBCO + 2-CABP
1rlc - tRBCO + 2-CABP

RuBisCO complex with productRuBisCO complex with product

1aa1 – spRBCO + phosphoglycerate
1rus - RrRBCO + phosphoglycerate

RuBisCO complex with substrateRuBisCO complex with substrate

1rcx, 1rxo – spRBCO + ribulose-1,5-bisphosphate
9rub - RrRBCO + ribulose-1,5-bisphosphate
1rsc - SeRBCO + xylulose-1,5-bisphosphate
1rco - spRBCO + xylulose-diol-1,5-bisphosphate
3zxw - SeRBCO + carboxyarabinitol-1,5-bisphosphate

RuBisCO complexesRuBisCO complexes

2h21 – pRBCO LSMT + AdoMet
2h23 - pRBCO LSMT + AdoHcy
2h2e, 1ozv, 1p0y - pRBCO LSMT + AdoMet + lysine
2h2j - pRBCO LSMT + sinefungin
2d69 – PhRBCO + sulfate
2rus - RrRBCO + CO2 + Mg
4f0h – GsRBCO + O2 – Galdieria sulphuraria
4f0k - GsRBCO + CO2 + Mg
4f0m - GsRBCO + Mg
1ej7 – tRBCO + phosphate
3axk – rRBCO + NADP
3axm – rRBCO + 6PG